ID A0A292YE04_9BACL Unreviewed; 667 AA.
AC A0A292YE04;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662, ECO:0000256|RuleBase:RU004996};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN ORFNames=EFBL_2494 {ECO:0000313|EMBL:GAX90852.1};
OS Effusibacillus lacus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Effusibacillus.
OX NCBI_TaxID=1348429 {ECO:0000313|EMBL:GAX90852.1, ECO:0000313|Proteomes:UP000217785};
RN [1] {ECO:0000313|Proteomes:UP000217785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skLN1 {ECO:0000313|Proteomes:UP000217785};
RA Watanabe M., Kojima H., Fukui M.;
RT "Draft genome sequence of Effusibacillus lacus strain skLN1.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027,
CC ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC {ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU004996};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU004996}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131, ECO:0000256|RuleBase:RU004996}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX90852.1}.
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DR EMBL; BDUF01000064; GAX90852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A292YE04; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000217785; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU004996};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004996};
KW Reference proteome {ECO:0000313|Proteomes:UP000217785};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 355..526
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 667 AA; 72723 MW; DF029E7549246812 CRC64;
MTTHSLEQLA INTIRTLSID GVDKANSGHP GMPMGAAPMA YVLWTRFMKH NPKNPSWFNR
DRFVLSAGHG SMLLYSLLHL CGYDVTMDDL KNFRQWGSRT PGHPEFGHTP GVEATTGPLG
QGISMAVGMA MAERHMAATY NRPGHELIAH YTYVICGDGD LMEGVASEAA SLAGHLKLGR
LIVLYDSNDI SLDGELNLSF SEDVSKRFEA YGWQVLRVED GNDTQAIEQA IAKAQEHTDQ
PTLIEVKTTI GFGSPNRAGS AEAHGKPLGS EEAKRTKENY QWPHEPFHVP EDVRQHFAKV
AEAGEKAEAE WQQGFDRYKR EFPELAKQFE LAVEGKLPAD WDAKLPKYTV DKGKIATRNA
SGDVLNAIAG TVPYFLGGSA DLASSNMTLL KGDSNFNAGD YSGRNMWFGV REHAMGAVLN
GMMLHGGLKV YGGTFFVFSD YLRPAMRLSA LMKVPVIYVM THDSIAVGED GPTHQPIEHL
AAMRVIPGMT VIRPADANET VGAYRYAVAD SKGPVTIVLS RQGLPVLEGT QDHIGEKVAR
GAYVISDSTD APQAILIATG SEVSLALKAQ QELTARGVSA RVVSMPSWEL FDKQPQAYKD
EVLPPHVKAR VAIEMGHPMG WERYVGDQGK VLGISQFGAS APGDKVIEEY GFTVQNVVSL
VEQTLEK
//
